MSRA_HUMAN
ID MSRA_HUMAN Reviewed; 235 AA.
AC Q9UJ68; E9PAS8; Q52TC4; Q549N4; Q66MI7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitochondrial peptide methionine sulfoxide reductase;
DE EC=1.8.4.11 {ECO:0000250|UniProtKB:Q9D6Y7};
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE AltName: Full=Protein-methionine-S-oxide reductase;
DE Short=PMSR;
DE Flags: Precursor;
GN Name=MSRA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=10452521; DOI=10.1016/s0014-5793(99)00917-5;
RA Kuschel L., Hansel A., Schoenherr R., Weissbach H., Brot N., Hoshi T.,
RA Heinemann S.H.;
RT "Molecular cloning and functional expression of a human peptide methionine
RT sulfoxide reductase (hMsrA).";
RL FEBS Lett. 456:17-21(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15680232; DOI=10.1016/j.bbapap.2004.09.010;
RA Hansel A., Heinemann S.H., Hoshi T.;
RT "Heterogeneity and function of mammalian MSRs: enzymes for repair,
RT protection and regulation.";
RL Biochim. Biophys. Acta 1703:239-247(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE PROMOTER USAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16364291; DOI=10.1016/j.exer.2005.10.003;
RA Lee J.W., Gordiyenko N.V., Marchetti M., Tserentsoodol N., Sagher D.,
RA Alam S., Weissbach H., Kantorow M., Rodriguez I.R.;
RT "Gene structure, localization and role in oxidative stress of methionine
RT sulfoxide reductase A (MSRA) in the monkey retina.";
RL Exp. Eye Res. 82:816-827(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] (ISOFORM 1).
RA Zhao Y., Yu L., Tu Q., Yue P., Zhang M., Zhao S.Y.;
RT "Cloning of a novel human cDNA which shows great homology to Bos taurus
RT methionine sulfoxide reductase (msrA) mRNA.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RA Peng Y., Huang C., Gu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "A novel gene expressed in human hypothalamus.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-6; ARG-7; ARG-22 AND
RP 11-LEU--LEU-14.
RX PubMed=12039877; DOI=10.1096/fj.01-0737fje;
RA Hansel A., Kuschel L., Hehl S., Lemke C., Agricola H.J., Hoshi T.,
RA Heinemann S.H.;
RT "Mitochondrial targeting of the human peptide methionine sulfoxide
RT reductase (MSRA), an enzyme involved in the repair of oxidized proteins.";
RL FASEB J. 16:911-913(2002).
RN [11]
RP MYRISTOYLATION AT GLY-2 (ISOFORM 5), AND ALTERNATIVE INITIATION.
RX PubMed=20368336; DOI=10.1074/jbc.m110.119701;
RA Kim G., Cole N.B., Lim J.C., Zhao H., Levine R.L.;
RT "Dual sites of protein initiation control the localization and
RT myristoylation of methionine sulfoxide reductase A.";
RL J. Biol. Chem. 285:18085-18094(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP MYRISTOYLATION AT GLY-2 (ISOFORM 5), CLEAVAGE OF INITIATOR METHIONINE
RP (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC Evidence={ECO:0000250|UniProtKB:Q9D6Y7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.11;
CC Evidence={ECO:0000250|UniProtKB:Q9D6Y7};
CC -!- INTERACTION:
CC Q9UJ68; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-19157918, EBI-11962928;
CC Q9UJ68; Q9BUY7: EFCAB11; NbExp=3; IntAct=EBI-19157918, EBI-18688654;
CC Q9UJ68; Q9UKT7: FBXL3; NbExp=3; IntAct=EBI-19157918, EBI-2557269;
CC Q9UJ68; Q9UM19: HPCAL4; NbExp=3; IntAct=EBI-19157918, EBI-744820;
CC Q9UJ68; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-19157918, EBI-10181968;
CC Q9UJ68; Q13228: SELENBP1; NbExp=3; IntAct=EBI-19157918, EBI-711619;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm. Membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=5;
CC Comment=Only about 25% of mRNAs are initiated at the mitochondrial
CC isoform 1 codon.;
CC Name=1; Synonyms=MsrA1, mitoMSRA, a;
CC IsoId=Q9UJ68-1; Sequence=Displayed;
CC Name=2; Synonyms=MsrA2, d;
CC IsoId=Q9UJ68-2; Sequence=VSP_041405;
CC Name=3; Synonyms=MsrA3, cytoMSRA, c;
CC IsoId=Q9UJ68-3; Sequence=VSP_041406;
CC Name=4; Synonyms=b;
CC IsoId=Q9UJ68-4; Sequence=VSP_041407;
CC Name=5;
CC IsoId=Q9UJ68-5; Sequence=VSP_042132;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in adult kidney and
CC cerebellum, followed by liver, heart ventricles, bone marrow and
CC hippocampus.
CC -!- MISCELLANEOUS: [Isoform 1]: Mitochondrial. Produced by alternative
CC splicing.
CC -!- MISCELLANEOUS: [Isoform 2]: Cytoplasmic. Produced by alternative
CC promoter usage. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Cytoplasmic and nuclear. Produced by
CC alternative promoter usage. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Cytoplasmic. Produced by alternative
CC initiation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC {ECO:0000305}.
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DR EMBL; AJ242973; CAB59628.1; -; mRNA.
DR EMBL; AY690665; AAU11088.1; -; mRNA.
DR EMBL; AY958429; AAY17426.1; -; mRNA.
DR EMBL; AY958430; AAY17427.1; -; mRNA.
DR EMBL; AY958431; AAY17428.1; -; mRNA.
DR EMBL; AY958432; AAY17429.1; -; Genomic_DNA.
DR EMBL; AY958432; AAY17430.1; -; Genomic_DNA.
DR EMBL; AY958432; AAY17431.1; -; Genomic_DNA.
DR EMBL; AK293488; BAH11521.1; -; mRNA.
DR EMBL; AF086925; AAP97154.1; -; mRNA.
DR EMBL; AF183420; AAG09689.1; -; mRNA.
DR EMBL; AC023385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471157; EAW65584.1; -; Genomic_DNA.
DR EMBL; CH471157; EAW65585.1; -; Genomic_DNA.
DR EMBL; BC054033; AAH54033.1; -; mRNA.
DR CCDS; CCDS47798.1; -. [Q9UJ68-4]
DR CCDS; CCDS47799.1; -. [Q9UJ68-3]
DR CCDS; CCDS56522.1; -. [Q9UJ68-2]
DR CCDS; CCDS5975.1; -. [Q9UJ68-1]
DR RefSeq; NP_001129142.1; NM_001135670.2. [Q9UJ68-4]
DR RefSeq; NP_001129143.1; NM_001135671.2. [Q9UJ68-3]
DR RefSeq; NP_001186658.1; NM_001199729.2. [Q9UJ68-2]
DR RefSeq; NP_036463.1; NM_012331.4. [Q9UJ68-1]
DR RefSeq; XP_016868938.1; XM_017013449.1. [Q9UJ68-2]
DR RefSeq; XP_016868939.1; XM_017013450.1. [Q9UJ68-2]
DR AlphaFoldDB; Q9UJ68; -.
DR SMR; Q9UJ68; -.
DR BioGRID; 110588; 29.
DR IntAct; Q9UJ68; 10.
DR MINT; Q9UJ68; -.
DR STRING; 9606.ENSP00000313921; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB00134; Methionine.
DR iPTMnet; Q9UJ68; -.
DR PhosphoSitePlus; Q9UJ68; -.
DR BioMuta; MSRA; -.
DR DMDM; 12230350; -.
DR EPD; Q9UJ68; -.
DR jPOST; Q9UJ68; -.
DR MassIVE; Q9UJ68; -.
DR MaxQB; Q9UJ68; -.
DR PaxDb; Q9UJ68; -.
DR PeptideAtlas; Q9UJ68; -.
DR PRIDE; Q9UJ68; -.
DR ProteomicsDB; 84588; -. [Q9UJ68-1]
DR ProteomicsDB; 84589; -. [Q9UJ68-2]
DR ProteomicsDB; 84590; -. [Q9UJ68-3]
DR ProteomicsDB; 84591; -. [Q9UJ68-4]
DR ProteomicsDB; 84592; -. [Q9UJ68-5]
DR Antibodypedia; 8418; 247 antibodies from 33 providers.
DR DNASU; 4482; -.
DR Ensembl; ENST00000317173.9; ENSP00000313921.4; ENSG00000175806.15. [Q9UJ68-1]
DR Ensembl; ENST00000382490.9; ENSP00000371930.5; ENSG00000175806.15. [Q9UJ68-3]
DR Ensembl; ENST00000441698.6; ENSP00000410912.2; ENSG00000175806.15. [Q9UJ68-4]
DR Ensembl; ENST00000528246.5; ENSP00000436839.1; ENSG00000175806.15. [Q9UJ68-2]
DR Ensembl; ENST00000643047.1; ENSP00000493922.1; ENSG00000285250.2. [Q9UJ68-3]
DR Ensembl; ENST00000643332.1; ENSP00000495223.1; ENSG00000285250.2. [Q9UJ68-4]
DR Ensembl; ENST00000645254.1; ENSP00000496174.1; ENSG00000285250.2. [Q9UJ68-2]
DR Ensembl; ENST00000645318.2; ENSP00000493848.1; ENSG00000285250.2. [Q9UJ68-1]
DR GeneID; 4482; -.
DR KEGG; hsa:4482; -.
DR MANE-Select; ENST00000317173.9; ENSP00000313921.4; NM_012331.5; NP_036463.1.
DR UCSC; uc003wsx.4; human. [Q9UJ68-1]
DR CTD; 4482; -.
DR DisGeNET; 4482; -.
DR GeneCards; MSRA; -.
DR HGNC; HGNC:7377; MSRA.
DR HPA; ENSG00000175806; Tissue enhanced (kidney, liver).
DR MIM; 601250; gene.
DR neXtProt; NX_Q9UJ68; -.
DR OpenTargets; ENSG00000175806; -.
DR PharmGKB; PA31182; -.
DR VEuPathDB; HostDB:ENSG00000175806; -.
DR eggNOG; KOG1635; Eukaryota.
DR GeneTree; ENSGT00390000003823; -.
DR HOGENOM; CLU_031040_10_3_1; -.
DR InParanoid; Q9UJ68; -.
DR OMA; AGPFYYA; -.
DR OrthoDB; 1383773at2759; -.
DR PhylomeDB; Q9UJ68; -.
DR TreeFam; TF353884; -.
DR BRENDA; 1.8.4.11; 2681.
DR PathwayCommons; Q9UJ68; -.
DR Reactome; R-HSA-5676934; Protein repair.
DR SignaLink; Q9UJ68; -.
DR BioGRID-ORCS; 4482; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; MSRA; human.
DR GeneWiki; MSRA_(gene); -.
DR GenomeRNAi; 4482; -.
DR Pharos; Q9UJ68; Tbio.
DR PRO; PR:Q9UJ68; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UJ68; protein.
DR Bgee; ENSG00000175806; Expressed in cortical plate and 100 other tissues.
DR ExpressionAtlas; Q9UJ68; baseline and differential.
DR Genevisible; Q9UJ68; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0006555; P:methionine metabolic process; TAS:ProtInc.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0030091; P:protein repair; TAS:Reactome.
DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR Pfam; PF01625; PMSR; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Alternative promoter usage;
KW Alternative splicing; Cytoplasm; Disulfide bond; Lipoprotein; Membrane;
KW Mitochondrion; Myristate; Nucleus; Oxidoreductase; Redox-active center;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT CHAIN 24..235
FT /note="Mitochondrial peptide methionine sulfoxide
FT reductase"
FT /id="PRO_0000138626"
FT ACT_SITE 74
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT MOD_RES 106
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D6Y7"
FT MOD_RES 106
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D6Y7"
FT DISULFID 74..220
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT DISULFID 220..229
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0A744"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16364291"
FT /id="VSP_041405"
FT VAR_SEQ 1..48
FT /note="MLSATRRACQLLLLHSLFPVPRMGNSASNIVSPQEALPGRKEQTPVAA ->
FT MCSEP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15680232,
FT ECO:0000303|PubMed:16364291"
FT /id="VSP_041406"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_042132"
FT VAR_SEQ 71..110
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_041407"
FT MUTAGEN 6
FT /note="R->A: Impaired subcellular location."
FT /evidence="ECO:0000269|PubMed:12039877"
FT MUTAGEN 7
FT /note="R->A: Impaired subcellular location."
FT /evidence="ECO:0000269|PubMed:12039877"
FT MUTAGEN 11..13
FT /note="Missing: Impaired subcellular location."
FT MUTAGEN 22
FT /note="R->A: Impaired subcellular location."
FT /evidence="ECO:0000269|PubMed:12039877"
FT CONFLICT 12..14
FT /note="Missing (in Ref. 6; AAG09689)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..137
FT /note="LKVF -> SRL (in Ref. 6; AAG09689)"
FT /evidence="ECO:0000305"
FT LIPID Q9UJ68-5:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20368336,
FT ECO:0000269|PubMed:25807930"
SQ SEQUENCE 235 AA; 26132 MW; B89A9BBBE4D58D90 CRC64;
MLSATRRACQ LLLLHSLFPV PRMGNSASNI VSPQEALPGR KEQTPVAAKH HVNGNRTVEP
FPEGTQMAVF GMGCFWGAER KFWVLKGVYS TQVGFAGGYT SNPTYKEVCS EKTGHAEVVR
VVYQPEHMSF EELLKVFWEN HDPTQGMRQG NDHGTQYRSA IYPTSAKQME AALSSKENYQ
KVLSEHGFGP ITTDIREGQT FYYAEDYHQQ YLSKNPNGYC GLGGTGVSCP VGIKK
